A comparison of the structure and properties of serum transferrin from 17 animal species.
1. A comparison of the chemical and physical properties of the iron transport protein transferrin, purified from the following seventeen animal sera, is reported; human, rhesus monkey, dog, cat, rabbit, guinea pig, mouse, rat, cow, sheep, goat, horse, pig, turkey, duck, turtle and rattlesnake. 2. Similarities and differences in molecular weight, isoelectric point, antibody specificity, effect of pH on iron release, number of sialic acid residues, amino acid composition and the N-terminal amino acid residue, are discussed. 3. The results are compared with the commonly accepted evolutionary origins of the 17 species.
Welch
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Department of Biochemistry, Faculty of Basic Medical Science, Queen Mary and Westfield College, London, UK.
D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D005075:Biological Evolution; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007120:Immunochemistry; D007501:Iron; D015394:Molecular Structure; D008970:Molecular Weight; D011489:Protein Denaturation; D012794:Sialic Acids / Q000737:chemistry; D013045:Species Specificity; D014168:Transferrin / Q000737:chemistry* / Q000235:genetics / Q000276:immunology
D000596:Amino Acids; D012794:Sialic Acids; D014168:Transferrin; D007501:Iron